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P24664

- TRYP_SACER

UniProt

P24664 - TRYP_SACER

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Protein

Trypsin

Gene
N/A
Organism
Saccharopolyspora erythraea (Streptomyces erythraeus)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei42 – 421Charge relay system
Active sitei88 – 881Charge relay system
Sitei173 – 1731Required for specificity By similarity
Active sitei179 – 1791Charge relay system

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.102.

Names & Taxonomyi

Protein namesi
Recommended name:
Trypsin (EC:3.4.21.4)
Alternative name(s):
SET
OrganismiSaccharopolyspora erythraea (Streptomyces erythraeus)
Taxonomic identifieri1836 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227TrypsinPRO_0000088718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 43
Disulfide bondi150 ↔ 164
Disulfide bondi175 ↔ 199

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

IntActiP24664. 1 interaction.
MINTiMINT-8289191.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113
Beta strandi15 – 195
Beta strandi25 – 339
Beta strandi36 – 394
Helixi41 – 444
Helixi49 – 513
Beta strandi53 – 575
Beta strandi66 – 7611
Helixi83 – 853
Beta strandi90 – 967
Helixi111 – 1133
Beta strandi118 – 12811
Beta strandi138 – 1447
Helixi147 – 1537
Turni159 – 1613
Beta strandi162 – 1654
Beta strandi182 – 1854
Beta strandi188 – 1958
Beta strandi197 – 2004
Beta strandi206 – 2105
Helixi211 – 2144
Helixi215 – 2228

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4M7GX-ray0.81A1-227[»]
ProteinModelPortaliP24664.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 223223Peptidase S1Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24664-1 [UniParc]FASTAAdd to Basket

« Hide

IVGGEDANVQ DHPFTVALVT PDGQQFCGGT LAAPNKVVTA AHCTVGSQPA    50
DINVVSGRTV MSSNIGTVSK VTNVWVHPEY QDAAKGFDVS VLTLEAPVKE 100
APIELAKADD AGYAPDTAAT ILGWGNTSEG GQQADHLQKA TVPVNSDDTC 150
KQAYGEYTPN AMVCAGVPEG GVDTCQGDSG GPMVVNNKLI GVTSWGEGCA 200
RPGKPGVYAR VGAYYDVLME QINAGAV 227
Length:227
Mass (Da):23,308
Last modified:March 1, 1992 - v1
Checksum:iD5AC5E47B227B418
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4M7G X-ray 0.81 A 1-227 [» ]
ProteinModelPortali P24664.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P24664. 1 interaction.
MINTi MINT-8289191.

Protein family/group databases

MEROPSi S01.102.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Miyamoto K., Matsuo H., Narita K.
    (In) Proceedings of Dai 30 kai tanpakushitsu kouzou touronkai kouen youshishuu, pp.77-80, Tokyo (1979)
    Cited for: PROTEIN SEQUENCE.
  2. "Crystal structure of Streptomyces erythraeus trypsin at 2.7-A resolution."
    Yamane T., Kobuke M., Tsutsui H., Toida T., Suzuki A., Ashida T., Kawata Y., Sakiyama F.
    J. Biochem. 110:945-950(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), SEQUENCE REVISION.

Entry informationi

Entry nameiTRYP_SACER
AccessioniPrimary (citable) accession number: P24664
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 11, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Hardly autolyzes itself at all at its active pH range.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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